cDNA Cloning and Expression of Blo t 11, the &lt;i&gt;Blomia tropicalis&lt;/i&gt; Allergen Homologous to Paramyosin

The examination of house dust mite extracts has indicated that over 30 different proteins can induce IgE antibody in patients allergic to the house dust mite. There are however dominant specificities especially the group 1 and 2 allergens which can account for much of the allergenicity of extracts. Of the 19 denominated allergens, the major IgE binding has been reported for the group 1, 2, 3, 9, 11, 14 and 15 allergens. The high-molecular-weight group 11, 14 and 15 allergens have only recently been described and although high IgE binding has been anticipated from immunoblotting, there is a need for considerable corroboration. Similarly, the study of the group 3 and 9 serine protease allergens has been incomplete. The group 4, 5, 7 and 8 allergens have shown intermediate IgE binding and the group 10 tropomyosins are of interest because of their potential cross-reactivity with allergen from disparate species. Although the progress with the production of recombinant group 1 allergens has been recent, many of the allergens can be produced as high IgE-binding polypeptides. The tertiary structure of the group 2 allergens has been determined from recombinant proteins and they are an excellent model for the investigation of modified allergens. An unexpected property of the group 1, 2 and 3 allergens has been the high degree of polymorphism found by cDNA analysis. It has however been possible to identify sequences to represent the variation in the natural allergens. The group 7 and 14 allergens show secondary modifications which vary in different extracts creating batch variation. While some estimate of the importance of allergens can be obtained from IgE binding, few analyses of T-cell responses have been made and these regulate both the development of, and the protection from sensitization.

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“…Blo t 11 from B. tropicalis has recently been examined. The 875-residue recombinant protein bound IgE in 50% of allergic sera [165]. …”

Section: Group 11 Allergensmentioning

confidence: 99%

Characterization and Immunobiology of House Dust Mite Allergens

Thomas¹,

Smith²,

Hales³

et al. 2002

Int Arch Allergy Immunol

301

254

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“…The first recombinant allergens were produced in Escherichia coli , resulting in nonglycosylated molecules [96, 97, 98, 99, 100, 101, 102]. This prokaryotic expression system is still applied for the production of many different recombinant allergens [103, 104, 105, 106, 107, 108]. In more recent years, several allergens were produced in eukaryotic expression systems like the yeast Pichia pastoris [109, 110, 111, 112, 113, 114, 115, 116, 117, 118, 119, 120, 121, 122, 123, 124, 125, 126, 127], insect cells [128, 129, 130, 131, 132, 133, 134, 135, 136], and tobacco plants [137, 138].…”

Section: Recombinant Allergens For Application In Diagnostics and Immmentioning

confidence: 99%

Carbohydrate Epitopes and Their Relevance for the Diagnosis and Treatment of Allergic Diseases

Ree¹

2002

Int Arch Allergy Immunol

173

119

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Allergenicity of plant and invertebrate N-glycans has been shown to be caused by the presence of two typical nonmammalian substitutions: an α(1,3)-fucose linked to the proximal N-acetylglucosamine and a β(1,2)-xylose linked to the core mannose. IgE antibodies against these carbohydrate structures are induced upon exposure to pollen or after insect stings, and result in extensive cross-reactivity to plant and invertebrate foods. These cross-reactive IgE antibodies have been shown to possess variable degrees of biological activity, but have never been convincingly shown to induce clinical food allergy. The most likely explanation for this lack of clinical relevance has to be sought in a combination of epitope valency and antibody affinity. In diagnostic tests, these antibodies are at the basis of many false-positive test results for food allergy. Recombinant technologies offer the possibility to produce allergens that do not carry IgE-binding glycans. Whether their absence or presence is of importance for the application of recombinant allergens in immunotherapy is still largely unknown.

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“…In a study investigating the mite fauna of 72 homes in different regions of Brazil, BLO was detected in 100% of the samples and accounted for 79.5% of the total number of mites found (Rosa & Flechtmann 1979). The most important allergens for humans are Blo t 3 (Cheong et al 2003), Blo t 5 (Arruda et al 1997), Blo t 11 (Ramos et al 2001), and Blo t 12 (Puerta et al 1996).…”

Section: Discussionmentioning

confidence: 99%

Serological identification of house dust mite allergens in dogs with atopic dermatitis

2012

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Pesq. Vet. Bras. 32(9):917-921, setembro 2012 917 RESUMO.-[Identiϐicação sorológica de alérgenos de ácaros da poeira domiciliar em cães com dermatite atópica.] Antígenos de ácaros da poeira domiciliar são utilizados por décadas para diagnóstico de doenças alér-gicas em seres humanos e animais. O objetivo do presente trabalho foi identiϐicar proteínas alergênicas presentes em extratos de Dermatophagoides farinae e Blomia tropicalis através de "immunoblotting" utilizando-se soros de animais alérgicos e conjugado anti-IgE canina. A análise por "immunoblotting" dos antígenos presentes no extrato de D. farinae (FDA Allergenic), utilizando soros de dez animais alérgicos, mostrou que oito soros reconhecem uma banda com peso molecular de aproximadamente 102 kDa; oito soros duas bandas entre 52 e 76 kDa; cinco soros uma banda com aproximadamente 76 kDa; quatro soros uma ban- House dust mite antigens have been used for decades to diagnose allergic diseases in humans and animals. The objective of this study was to identify allergens in commercial Dermatophagoides farinae and Blomia tropicalis extracts by immunoblotting using sera from allergic dogs and anti-dog IgE conjugate. The analysis of antigens present in the D. farinae extract (FDA Allergenic) using sera from 10 dogs allergic to D. farinae showed that eight sera recognized a band of approximately 102 kDa, eight recognized two bands of 52 to 76 kDa, ϐive recognized one band of approximately 76 kDa, four recognized one band of 31 to 38 kDa, and two recognized one band of 12 to 17 kDa. Immunoblot assays of the B. tropicalis extract (FDA Allergenic) using sera from 10 animals allergic to B. tropicalis showed that ϐive sera recognized two bands of 52 to 76 kDa. These results demonstrate the importance of the two house dust mite species for the pathogenesis of canine atopic dermatitis in Brazil. In addition, the results indicate which allergens should be present in allergenic extracts used for diagnosis and allergen-speciϐic immunotherapy. da entre 31 e 38 kDa; e dois soros uma banda entre 12 e 17 kDa. A análise por "immunoblotting" dos antígenos do extrato de B. tropicalis (FDA Allergenic) mostrou que cinco soros reconhecem duas bandas com pesos moleculares entre 52 e 76 kDa. Esses resultados demonstram a importância dessas duas espécies de ácaros da poeira domiciliar na patogênese da dermatite atópica canina no Brasil, assim como indicam alérgenos que devem estar presentes nos extratos alergênicos utilizados para diagnóstico e imunoterapia alérgeno-especíϐica.

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cDNA Cloning and Expression of Blo t 11, the <i>Blomia tropicalis</i> Allergen Homologous to Paramyosin

Cited by 45 publications

References 23 publications

Characterization and Immunobiology of House Dust Mite Allergens

Characterization and Immunobiology of House Dust Mite Allergens

Carbohydrate Epitopes and Their Relevance for the Diagnosis and Treatment of Allergic Diseases

Serological identification of house dust mite allergens in dogs with atopic dermatitis

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